E70A1_ARATH
ID E70A1_ARATH Reviewed; 638 AA.
AC Q9LZD3;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Exocyst complex component EXO70A1 {ECO:0000303|PubMed:16942608};
DE Short=AtExo70a1 {ECO:0000303|PubMed:16942608};
DE AltName: Full=Exocyst subunit Exo70 family protein A1 {ECO:0000303|PubMed:16942608};
GN Name=EXO70A1 {ECO:0000303|PubMed:16942608};
GN OrderedLocusNames=At5g03540 {ECO:0000312|Araport:AT5G03540};
GN ORFNames=F12E4.320 {ECO:0000312|EMBL:CAB83315.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16942608; DOI=10.1111/j.1365-313x.2006.02854.x;
RA Synek L., Schlager N., Elias M., Quentin M., Hauser M.-T., Zarsky V.;
RT "AtEXO70A1, a member of a family of putative exocyst subunits specifically
RT expanded in land plants, is important for polar growth and plant
RT development.";
RL Plant J. 48:54-72(2006).
RN [5]
RP COMPONENT OF THE EXOCYST COMPLEX.
RX PubMed=18492870; DOI=10.1105/tpc.108.059105;
RA Hala M., Cole R., Synek L., Drdova E., Pecenkova T., Nordheim A.,
RA Lamkemeyer T., Madlung J., Hochholdinger F., Fowler J.E., Zarsky V.;
RT "An exocyst complex functions in plant cell growth in Arabidopsis and
RT tobacco.";
RL Plant Cell 20:1330-1345(2008).
RN [6]
RP GENE FAMILY, NOMENCLATURE, AND SUBCELLULAR LOCATION.
RX PubMed=19895414; DOI=10.1111/j.1469-8137.2009.03070.x;
RA Chong Y.T., Gidda S.K., Sanford C., Parkinson J., Mullen R.T., Goring D.R.;
RT "Characterization of the Arabidopsis thaliana exocyst complex gene families
RT by phylogenetic, expression profiling, and subcellular localization
RT studies.";
RL New Phytol. 185:401-419(2010).
RN [7]
RP FUNCTION.
RX PubMed=20618910; DOI=10.1111/j.1469-8137.2010.03372.x;
RA Kulich I., Cole R., Drdova E., Cvrckova F., Soukup A., Fowler J.,
RA Zarsky V.;
RT "Arabidopsis exocyst subunits SEC8 and EXO70A1 and exocyst interactor ROH1
RT are involved in the localized deposition of seed coat pectin.";
RL New Phytol. 188:615-625(2010).
RN [8]
RP FUNCTION, INTERACTION WITH EXO84B, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20870962; DOI=10.1105/tpc.110.074351;
RA Fendrych M., Synek L., Pecenkova T., Toupalova H., Cole R., Drdova E.,
RA Nebesarova J., Sedinova M., Hala M., Fowler J.E., Zarsky V.;
RT "The Arabidopsis exocyst complex is involved in cytokinesis and cell plate
RT maturation.";
RL Plant Cell 22:3053-3065(2010).
RN [9]
RP INTERACTION WITH SEC3A.
RX PubMed=23495664; DOI=10.1111/nph.12236;
RA Zhang Y., Immink R., Liu C.M., Emons A.M., Ketelaar T.;
RT "The Arabidopsis exocyst subunit SEC3A is essential for embryo development
RT and accumulates in transient puncta at the plasma membrane.";
RL New Phytol. 199:74-88(2013).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23709627; DOI=10.1105/tpc.113.112144;
RA Li S., Chen M., Yu D., Ren S., Sun S., Liu L., Ketelaar T., Emons A.M.,
RA Liu C.M.;
RT "EXO70A1-mediated vesicle trafficking is critical for tracheary element
RT development in Arabidopsis.";
RL Plant Cell 25:1774-1786(2013).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23163883; DOI=10.1111/tpj.12074;
RA Drdova E.J., Synek L., Pecenkova T., Hala M., Kulich I., Fowler J.E.,
RA Murphy A.S., Zarsky V.;
RT "The exocyst complex contributes to PIN auxin efflux carrier recycling and
RT polar auxin transport in Arabidopsis.";
RL Plant J. 73:709-719(2013).
RN [12]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=25541219; DOI=10.1093/pcp/pcu197;
RA Oda Y., Iida Y., Nagashima Y., Sugiyama Y., Fukuda H.;
RT "Novel coiled-coil proteins regulate exocyst association with cortical
RT microtubules in xylem cells via the conserved oligomeric golgi-complex 2
RT protein.";
RL Plant Cell Physiol. 56:277-286(2015).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=27801942; DOI=10.1111/nph.14267;
RA Vukasinovic N., Oda Y., Pejchar P., Synek L., Pecenkova T., Rawat A.,
RA Sekeres J., Potocky M., Zarsky V.;
RT "Microtubule-dependent targeting of the exocyst complex is necessary for
RT xylem development in Arabidopsis.";
RL New Phytol. 213:1052-1067(2017).
CC -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC exocytic vesicles with fusion sites on the plasma membrane during
CC regulated or polarized secretion. Involved in polarized cell growth and
CC organ morphogenesis. Involved in polarized cell growth and organ
CC morphogenesis. During cytokinesis, involved in cell plate initiation,
CC cell plate maturation and formation of new primary cell wall.
CC Participates in polarized pectin delivery required for the polarized
CC development of the mucilage-producing volcano cells of the seed coat.
CC Involved in the recycling and localization of auxin efflux carriers
CC PIN1 and PIN2, and thus in polar auxin transport regulation. Functions
CC in vesicle trafficking in tracheary elements to regulate patterned
CC secondary cell wall (SCW) thickening (PubMed:27801942).
CC {ECO:0000269|PubMed:16942608, ECO:0000269|PubMed:20618910,
CC ECO:0000269|PubMed:20870962, ECO:0000269|PubMed:23163883,
CC ECO:0000269|PubMed:23709627, ECO:0000269|PubMed:27801942}.
CC -!- SUBUNIT: The exocyst complex is composed of SEC3, SEC5, SEC6, SEC8,
CC SEC10, EXO70A1 and EXO84B. Interacts with SEC3A and EXO84B. Co-
CC localizes with FPP3/VETH1, FPP2/VETH2 and COG2 in vesicle-like small
CC motile compartments (PubMed:25541219). May interact with COG2
CC (PubMed:27801942). {ECO:0000269|PubMed:20870962,
CC ECO:0000269|PubMed:23495664, ECO:0000269|PubMed:25541219,
CC ECO:0000269|PubMed:27801942}.
CC -!- INTERACTION:
CC Q9LZD3; Q94AI6: SEC6; NbExp=3; IntAct=EBI-1797218, EBI-1797182;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19895414}.
CC Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:20870962}.
CC Cell membrane {ECO:0000269|PubMed:23163883}. Secreted, cell wall
CC {ECO:0000269|PubMed:20870962}. Note=During cytokinesis, localizes to
CC the nascent cell plate and later to the cell plate insertion site and
CC along the post-cytokinetic wall (PubMed:20870962). Localized at
CC vesicle-like small compartments at cortical microtubules, especially in
CC the presence of FPP3/VETH1, FPP2/VETH2 and COG2 (PubMed:25541219).
CC Confined to helical/annular plasma membrane (PM) domains in protoxylem
CC of roots before the secondary cell wall (SCW) is deposited. After the
CC induction of xylem differentiation, first associated with plasma
CC membrane (PM) foci and later co-localizes with microtubules (MT)
CC organized into regular bundles, especially at the cell cortex
CC (PubMed:27801942). {ECO:0000269|PubMed:20870962,
CC ECO:0000269|PubMed:25541219, ECO:0000269|PubMed:27801942}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LZD3-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Dwarf and sterile plants with decreased apical
CC dominance. Branched inflorescences due to ectopic initiation of lateral
CC inflorescences instead of flowers. Altered polar growth of root hairs
CC and stigmatic papillae. Reduced cell expansion and aberrant xylem
CC development. Aberrant deposition of xylem secondary cell wall (SCW)
CC (PubMed:27801942). {ECO:0000269|PubMed:16942608,
CC ECO:0000269|PubMed:20870962, ECO:0000269|PubMed:23709627,
CC ECO:0000269|PubMed:27801942}.
CC -!- SIMILARITY: Belongs to the EXO70 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL162751; CAB83315.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90620.1; -; Genomic_DNA.
DR EMBL; AY072155; AAL59977.1; -; mRNA.
DR EMBL; AY133751; AAM91685.1; -; mRNA.
DR PIR; T48380; T48380.
DR RefSeq; NP_195974.2; NM_120434.5. [Q9LZD3-1]
DR PDB; 4RL5; X-ray; 3.10 A; A/B=75-638.
DR PDBsum; 4RL5; -.
DR AlphaFoldDB; Q9LZD3; -.
DR SMR; Q9LZD3; -.
DR BioGRID; 17085; 10.
DR IntAct; Q9LZD3; 4.
DR STRING; 3702.AT5G03540.3; -.
DR TCDB; 1.F.2.1.3; the octameric exocyst (exocyst) family.
DR iPTMnet; Q9LZD3; -.
DR PaxDb; Q9LZD3; -.
DR PRIDE; Q9LZD3; -.
DR ProteomicsDB; 222035; -. [Q9LZD3-1]
DR DNASU; 831809; -.
DR EnsemblPlants; AT5G03540.1; AT5G03540.1; AT5G03540. [Q9LZD3-1]
DR GeneID; 831809; -.
DR Gramene; AT5G03540.1; AT5G03540.1; AT5G03540. [Q9LZD3-1]
DR KEGG; ath:AT5G03540; -.
DR Araport; AT5G03540; -.
DR eggNOG; KOG2344; Eukaryota.
DR OMA; GPIYGNT; -.
DR PhylomeDB; Q9LZD3; -.
DR PRO; PR:Q9LZD3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZD3; baseline and differential.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0090059; P:protoxylem development; IMP:UniProtKB.
DR GO; GO:0060178; P:regulation of exocyst localization; IDA:UniProtKB.
DR GO; GO:2000652; P:regulation of secondary cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:0010089; P:xylem development; IMP:UniProtKB.
DR GO; GO:0048759; P:xylem vessel member cell differentiation; IMP:UniProtKB.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR004140; Exo70.
DR InterPro; IPR046364; Exo70_C.
DR PANTHER; PTHR12542; PTHR12542; 1.
DR Pfam; PF03081; Exo70; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell wall; Cytoplasm;
KW Cytoskeleton; Exocytosis; Membrane; Reference proteome; Secreted;
KW Transport.
FT CHAIN 1..638
FT /note="Exocyst complex component EXO70A1"
FT /id="PRO_0000424565"
FT REGION 163..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 103..115
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 128..132
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 134..152
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 225..245
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 260..291
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 301..319
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 346..353
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 359..388
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 403..415
FT /evidence="ECO:0007829|PDB:4RL5"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 419..423
FT /evidence="ECO:0007829|PDB:4RL5"
FT TURN 428..430
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 436..456
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 464..483
FT /evidence="ECO:0007829|PDB:4RL5"
FT TURN 486..491
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 494..521
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 546..566
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 574..596
FT /evidence="ECO:0007829|PDB:4RL5"
FT HELIX 617..622
FT /evidence="ECO:0007829|PDB:4RL5"
FT STRAND 625..627
FT /evidence="ECO:0007829|PDB:4RL5"
SQ SEQUENCE 638 AA; 72299 MW; 4660A819EA0C8BB2 CRC64;
MAVDSRMDLL SERAVLMRAS LQKSQTITDN VVSILGSFDS RLSALETAMR PTQIRTHAIR
KAHENIDRTL KAAEVILSQF DLLRQAETKV LKGPHEDLES YLDAIAQLRK IIRYFMSNKS
FKSSDGVLNH ANSLLAKAQS KLEEEFKQLL ASYSKAVEPD RLFDGLPNSL RPSSDGDGGG
KPHGGHHNDD AETAAYTLPI LIPSRVLPLL HDLAQQMVQA GHQQQLLQIY RDTRSFVLEE
SLKKLGVEKL SKEDVQRMQW EVLEAKIGNW IHFMRIAVKL LFAGERQVCD QIFRGFDSLS
DQCFAEVTVS SVSMLLSFGD AIARSKRSPE KLFVLLDMYE IMRELHTEIE TIFKGKACLE
IRDSATGLTK RLAQTAQETF GDFEEAVEKD ATKTAVLDGT VHPLTSYVIN YVKFLFDYQT
TLKQLFLEFG NGDDSNSQLA SVTMRIMQAL QNNLDGKSKQ YKDPALTHLF LMNNIHYMVR
SVRRSEAKDL LGDDWVQRHR RIVQQHANQY KRVAWTKILQ SSSAQGLTSS GGGSLEGGNS
SGVSRGLLKE RFKMFNMQFD ELHQRQSQWT VPDTELRESL RLAVAEVLLP AYRSFLKRFG
PLVESGKNPQ KYIKYTAEDL ERLLGELFEG KSMNEPRR
